» Articles » PMID: 32695272

Directed Evolution of the Aryl-alcohol Oxidase: Beyond the Lab Bench

Overview
Specialty Biotechnology
Date 2020 Jul 23
PMID 32695272
Citations 4
Authors
Affiliations
Soon will be listed here.
Abstract

Aryl-alcohol oxidase (AAO) is a fungal GMC flavoprotein secreted by white-rot fungi that supplies HO to the ligninolytic consortium. This enzyme can oxidize a wide array of aromatic alcohols in a highly enantioselective manner, an important trait in organic synthesis. The best strategy to adapt AAO to industrial needs is to engineer its properties by directed evolution, aided by computational analysis. The aim of this review is to describe the strategies and challenges we faced when undertaking laboratory evolution of AAO. After a comprehensive introduction into the structure of AAO, its function and potential applications, the different directed evolution enterprises designed to express the enzyme in an active and soluble form in yeast are described, as well as those to unlock new activities involving the oxidation of secondary aromatic alcohols and the synthesis of furandicarboxylic acids.

Citing Articles

Multicopper oxidases with laccase-ferroxidase activity: Classification and study of ferroxidase activity determinants in a member from .

Aza P, Molpeceres G, Vind J, Camarero S Comput Struct Biotechnol J. 2023; 21:1041-1053.

PMID: 36733701 PMC: 9880977. DOI: 10.1016/j.csbj.2023.01.030.


Two adjacent C-terminal mutations enable expression of aryl-alcohol oxidase from Pleurotus eryngii in Pichia pastoris.

Jankowski N, Urlacher V, Koschorreck K Appl Microbiol Biotechnol. 2021; 105(20):7743-7755.

PMID: 34545417 PMC: 8502153. DOI: 10.1007/s00253-021-11585-4.


Pecularities and applications of aryl-alcohol oxidases from fungi.

Urlacher V, Koschorreck K Appl Microbiol Biotechnol. 2021; 105(10):4111-4126.

PMID: 33997930 PMC: 8140971. DOI: 10.1007/s00253-021-11337-4.


High-level expression of aryl-alcohol oxidase 2 from Pleurotus eryngii in Pichia pastoris for production of fragrances and bioactive precursors.

Jankowski N, Koschorreck K, Urlacher V Appl Microbiol Biotechnol. 2020; 104(21):9205-9218.

PMID: 32949280 PMC: 7567689. DOI: 10.1007/s00253-020-10878-4.

References
1.
Vrielink A, Ghisla S . Cholesterol oxidase: biochemistry and structural features. FEBS J. 2009; 276(23):6826-43. DOI: 10.1111/j.1742-4658.2009.07377.x. View

2.
Alcalde M . Engineering the ligninolytic enzyme consortium. Trends Biotechnol. 2015; 33(3):155-62. DOI: 10.1016/j.tibtech.2014.12.007. View

3.
Vina-Gonzalez J, Gonzalez-Perez D, Alcalde M . Directed Evolution Method in Saccharomyces cerevisiae: Mutant Library Creation and Screening. J Vis Exp. 2016; (110):e53761. PMC: 4841332. DOI: 10.3791/53761. View

4.
Caldwell J . Do single enantiomers have something special to offer?. Hum Psychopharmacol. 2002; 16(S2):S67-S71. DOI: 10.1002/hup.339. View

5.
Hernandez-Ortega A, Lucas F, Ferreira P, Medina M, Guallar V, Martinez A . Role of active site histidines in the two half-reactions of the aryl-alcohol oxidase catalytic cycle. Biochemistry. 2012; 51(33):6595-608. DOI: 10.1021/bi300505z. View